Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957   1 MKKLCILKLGSTYETLKIQSGDFEDWIVSVLDISRDEIEIVDPRNGVPI-DIEKYGAFISTGSHSMLSEEGEYAEYLSGI 79
Cdd:PRK09065   1 VKPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQPVVVVRVFAGEPLpAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  80 VSRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNGLEAGIVDIITTPEAKNDKIFGLLPGVFQAFAIHSQTILKPSPKIT 159
Cdd:PRK09065  81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504669957 160 RLAYNEFENHHAIRVGENAWGVQFHPEFTPFIMGEYLRQE 199
Cdd:PRK09065 161 VLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRAR 200

glutamine amidotransferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957   1 MKKLCILKLGSTYETLKIQSGDFEDWIVSVLDISRDEIEIVDPRNGVPI-DIEKYGAFISTGSHSMLSEEGEYAEYLSGI 79
Cdd:PRK09065   1 VKPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQPVVVVRVFAGEPLpAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  80 VSRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNGLEAGIVDIITTPEAKNDKIFGLLPGVFQAFAIHSQTILKPSPKIT 159
Cdd:PRK09065  81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504669957 160 RLAYNEFENHHAIRVGENAWGVQFHPEFTPFIMGEYLRQE 199
Cdd:PRK09065 161 VLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRAR 200

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957   3 KLCILKLGSTYETlkiqsGDFEDWIVSvLDISRDEIEIVDPRNGVPI-DIEKYGAFISTGSHSMLSEEGE-YAEYLSGIV 80
Cdd:cd01741    1 RILILQHDTPEGP-----GLFEDLLRE-AGAETIEIDVVDVYAGELLpDLDDYDGLVILGGPMSVDEDDYpWLKKLKELI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  81 SRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNGLEAGIVDIITTPEAKNDKIFGLLPGVFQAFAIHSQTILKPSPKITR 160
Cdd:cd01741   75 RQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELPPGAVL 154

                        170       180
                 ....*....|....*....|....*.
gi 504669957 161 LAYNEFENHHAIRVGENAWGVQFHPE 186
Cdd:cd01741  155 LASSEACPNQAFRYGDRALGLQFHPE 180

Glutamine amidotransferase class-I;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957   79 IVSRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNGLEAGIV-DIITTPEAKNDKifglLPGVFQAFAIHS----QTILK 153
Cdd:pfam00117  62 AIREARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHGKNsPVGDDGCGLFYG----LPNVFIVRRYHSyavdPDTLP 137

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 504669957  154 PSPKITRLAYNEFENHHAIRVGENAWGVQFHPEFTP 189
Cdd:pfam00117 138 DGLEVTATSENDGTIMGIRHKKLPIFGVQFHPESIL 173

glutamine amidotransferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957   1 MKKLCILKLGSTYETLKIQSGDFEDWIVSVLDISRDEIEIVDPRNGVPI-DIEKYGAFISTGSHSMLSEEGEYAEYLSGI 79
Cdd:PRK09065   1 VKPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQPVVVVRVFAGEPLpAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  80 VSRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNGLEAGIVDIITTPEAKNDKIFGLLPGVFQAFAIHSQTILKPSPKIT 159
Cdd:PRK09065  81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504669957 160 RLAYNEFENHHAIRVGENAWGVQFHPEFTPFIMGEYLRQE 199
Cdd:PRK09065 161 VLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRAR 200

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957   3 KLCILKLGSTYETlkiqsGDFEDWIVSvLDISRDEIEIVDPRNGVPI-DIEKYGAFISTGSHSMLSEEGE-YAEYLSGIV 80
Cdd:cd01741    1 RILILQHDTPEGP-----GLFEDLLRE-AGAETIEIDVVDVYAGELLpDLDDYDGLVILGGPMSVDEDDYpWLKKLKELI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  81 SRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNGLEAGIVDIITTPEAKNDKIFGLLPGVFQAFAIHSQTILKPSPKITR 160
Cdd:cd01741   75 RQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELPPGAVL 154

                        170       180
                 ....*....|....*....|....*.
gi 504669957 161 LAYNEFENHHAIRVGENAWGVQFHPE 186
Cdd:cd01741  155 LASSEACPNQAFRYGDRALGLQFHPE 180

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  39 EIVDprNGVPIDIEK----YGAFISTGSHSmlseegEYAEYLSGIVSRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNG 114
Cdd:cd01742   26 EILP--NTTPLEEIKlknpKGIILSGGPSS------VYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKR 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504669957 115 lEAGIVDIITTpeaKNDKIFGLLPGVFQAFAIHSQTILKPSPKITRLAYNefENHH--AIR-VGENAWGVQFHPE 186
Cdd:cd01742   98 -EYGKAEIEID---DSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASS--DNCPvaAIAnEEKKIYGVQFHPE 166

glutamine amidotransferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  80 VSRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNGL-EAGIVDIITTPEAKndkifGLLPGVFQAFAIHSQTILKPSpKI 158
Cdd:PRK06490  79 ISVPLKENKPFLGICLGAQMLARHLGARVAPHPDGRvEIGYYPLRPTEAGR-----ALMHWPEMVYHWHREGFDLPA-GA 152

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504669957 159 TRLAYNE-FENHhAIRVGENAWGVQFHPEFTPFIM 192
Cdd:PRK06490 153 ELLATGDdFPNQ-AFRYGDNAWGLQFHPEVTRAMM 186

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  76 LSGIVSRILDSNIPYFGICYGHQLLAKAAGCQIGF--NPNGleaGIVDIITTpeaKNDKIFGLLPGVFQAFAIHSQTILK 153
Cdd:cd01743   60 ISLEIIRALAGKVPILGVCLGHQAIAEAFGGKVVRapEPMH---GKTSEIHH---DGSGLFKGLPQPFTVGRYHSLVVDP 133

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504669957 154 PS-PKITRLAYNEFENH-HAIR-VGENAWGVQFHPE 186
Cdd:cd01743  134 DPlPDLLEVTASTEDGViMALRhRDLPIYGVQFHPE 169

anthranilate synthase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  77 SGI---VSRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNGLEAGIVDIITTPEAKNDKIFGLLPGVFQAFAIHSQTILK 153
Cdd:PLN02335  78 SGIslqTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSPVHYDEKGEEGLFSGLPNPFTAGRYHSLVIEK 157

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504669957 154 ---PSPKITRLAYNEFENHHAIRVGENAW--GVQFHPE 186
Cdd:PLN02335 158 dtfPSDELEVTAWTEDGLIMAARHRKYKHiqGVQFHPE 195

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504669957  40 IVDPRNGVPIDIEKY---GAFISTGShsmlseeG--EYAEYLSGIVSRILDSNIPYFGICYGHQLLAKAAGCQI 108
Cdd:cd01744   24 TVVPYNTDAEEILKLdpdGIFLSNGP-------GdpALLDEAIKTVRKLLGKKIPIFGICLGHQLLALALGAKT 90

carbamoyl-phosphate synthase small subunit;

                         10        20
                 ....*....|....*....|....*.
gi 504669957  83 ILDSNIPYFGICYGHQLLAKAAGCQI 108
Cdd:PRK12564 244 LLEKKIPIFGICLGHQLLALALGAKT 269

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  21 GDFEDWIVSVLDISRD---EIEIVDPRNGVP---IDIEKYGAFISTGSHSMLSEEGEYAEYLSGIVsRILDSNIPYFGIC 94
Cdd:cd03128    8 GSEELELASPLDALREagaEVDVVSPDGGPVesdVDLDDYDGLILPGGPGTPDDLAWDEALLALLR-EAAAAGKPVLGIC 86

                 ....*.
gi 504669957  95 YGHQLL 100
Cdd:cd03128   87 LGAQLL 92

amidotransferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  37 EIEIVDPRNGV-PIDIEKYGAFISTGSHSMLSEEGEYAEYLSGIVSRILDSNIPYFGICYGHQLLAKAAGCQIGFNPNGL 115
Cdd:PRK05665  40 EFVVYNVVQGDyPADDEKFDAYLVTGSKADSFGTDPWIQTLKTYLLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGW 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504669957 116 EAGIVDIITTPEAKndkifGLLPGV--FQAFAIHSQTILKPSPKITRLAYNEFENHHAIRVGENAWGVQFHPEF 187
Cdd:PRK05665 120 GVGIHRYQLAAHAP-----WMSPAVteLTLLISHQDQVTALPEGATVIASSDFCPFAAYHIGDQVLCFQGHPEF 188

carbamoyl phosphate synthase small subunit; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  41 VDPRNGVPIDIEKY---GAFISTGShsmlSEEGEYAEYLSGIvsRILDSNIPYFGICYGHQLLAKAAGCQI---GFNPNG 114
Cdd:PRK12838 194 VLPYDTSLEEIKNLnpdGIVLSNGP----GDPKELQPYLPEI--KKLISSYPILGICLGHQLIALALGADTeklPFGHRG 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957 115 LEAGIVDIITTPeakndkifgllpgVFQAFAIHSQTILKPSpkitrLAYNEFE------NHHAIR----VGENAWGVQFH 184
Cdd:PRK12838 268 ANHPVIDLTTGR-------------VWMTSQNHGYVVDEDS-----LDGTPLSvrffnvNDGSIEglrhKKKPVLSVQFH 329

                 ....*
gi 504669957 185 PEFTP 189
Cdd:PRK12838 330 PEAHP 334

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504669957   40 IVDPRNGVPIDIEKY---GAFISTGShsmlseeGEYA--EYLSGIVSRILdSNIPYFGICYGHQLLAKAAG 105
Cdd:TIGR01368 198 TVVPYDTDAEEIKKYnpdGIFLSNGP-------GDPAavEPAIETIRKLL-EKIPIFGICLGHQLLALAFG 260

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957   88 IPYFGICYGHQLLAKAAGCQIGFNPNGLEAGIVDIittpEAKNDKIFGLLPGVFQAFAIHSqTILKPS--PKITRLAYNE 165
Cdd:TIGR00566  73 LPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEI----EHNGAGIFRGLFNPLTATRYHS-LVVEPEtlPTCFPVTAWE 147

                          90       100
                  ....*....|....*....|....
gi 504669957  166 FENHH--AIRVGENAW-GVQFHPE 186
Cdd:TIGR00566 148 EENIEimAIRHRDLPLeGVQFHPE 171

aminodeoxychorismate synthase component 2;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504669957  88 IPYFGICYGHQLLAKAAGcqigfnpngleAGIVDIITTPEAKNDKIFGLLPGVFQAFA-------IHSQTILKPS-PKIT 159
Cdd:PRK08007  73 LPILGVCLGHQAMAQAFG-----------GKVVRAAKVMHGKTSPITHNGEGVFRGLAnpltvtrYHSLVVEPDSlPACF 141

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504669957 160 RL-AYNEFENHHAIRvgENAW---GVQFHPE 186
Cdd:PRK08007 142 EVtAWSETREIMGIR--HRQWdleGVQFHPE 170